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Volumn 21, Issue 4, 1996, Pages 871-884

New components of protein folding in extracytoplasmic compartments of escherichia coli SurA, FkpA and Skp/OmpH

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; OUTER MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; FKPA PROTEIN; OUTER MEMBRANE PROTEIN H; PEPTIDYLPROLYL ISOMERASE; SURA PROTEIN; UNCLASSIFIED DRUG;

EID: 0029765609     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1996.561412.x     Document Type: Article
Times cited : (299)

References (55)
  • 1
    • 0024728138 scopus 로고
    • Expression, purification and enzymatic characterization of a protein A-β-lactamase hybrid protein
    • Baneuyx, F., and Georgiou, G. (1989) Expression, purification and enzymatic characterization of a protein A-β-lactamase hybrid protein. Enzyme Microbiol Technol 11: 559-567.
    • (1989) Enzyme Microbiol Technol , vol.11 , pp. 559-567
    • Baneuyx, F.1    Georgiou, G.2
  • 2
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • Bardwell, J.C.A. (1994) Building bridges: disulphide bond formation in the cell. Mol Microbiol 14: 199-205.
    • (1994) Mol Microbiol , vol.14 , pp. 199-205
    • Bardwell, J.C.A.1
  • 3
    • 0029923189 scopus 로고    scopus 로고
    • Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies
    • Betton, J.-M., and Hofnung, M. (1996) Folding of a mutant maltose-binding protein of Escherichia coli which forms inclusion bodies. J Biol Chem 271: 8046-8052.
    • (1996) J Biol Chem , vol.271 , pp. 8046-8052
    • Betton, J.-M.1    Hofnung, M.2
  • 4
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • Chen, R., and Henning, U. (1996) A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol 19: 1287-1294.
    • (1996) Mol Microbiol , vol.19 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 5
    • 0027494834 scopus 로고
    • Nitrogenase metalloclusters: Structures, organization and synthesis
    • Dean, D.R., Bolin, J.T., and Zheng, L. (1993) Nitrogenase metalloclusters: structures, organization and synthesis. J Bacteriol 175: 6737-6744.
    • (1993) J Bacteriol , vol.175 , pp. 6737-6744
    • Dean, D.R.1    Bolin, J.T.2    Zheng, L.3
  • 6
    • 0025961131 scopus 로고
    • Cloning and nucleotide sequence of the firA gene and the firA200 (Ts) allele from Escherichia coli
    • Dicker, I.B., and Seetharam, S. (1991) Cloning and nucleotide sequence of the firA gene and the firA200 (Ts) allele from Escherichia coli. J Bacteriol 173: 334-344.
    • (1991) J Bacteriol , vol.173 , pp. 334-344
    • Dicker, I.B.1    Seetharam, S.2
  • 7
    • 0024519112 scopus 로고
    • DNA sequence of mip, a Legionella pneumophila gene associated with macrophage infectivity
    • Engleberg, N.C., Carter, C., Weber, D.R., Cianciotto, N.P., and Eisenstein, B.I. (1989) DNA sequence of mip, a Legionella pneumophila gene associated with macrophage infectivity. Infect Immun 57: 1263-1270.
    • (1989) Infect Immun , vol.57 , pp. 1263-1270
    • Engleberg, N.C.1    Carter, C.2    Weber, D.R.3    Cianciotto, N.P.4    Eisenstein, B.I.5
  • 8
    • 0023272340 scopus 로고
    • Interposon mutagenesis of soil and water bacteria: A family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria
    • Fellay, R., Frey, J., and Krisch, H. (1987) Interposon mutagenesis of soil and water bacteria: a family of DNA fragments designed for in vitro insertional mutagenesis of Gram-negative bacteria. Gene 52: 147-154.
    • (1987) Gene , vol.52 , pp. 147-154
    • Fellay, R.1    Frey, J.2    Krisch, H.3
  • 9
    • 0026511332 scopus 로고
    • Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity
    • Fischer, G., Bang, H., Ludwig, B., Mann, K., and Hacker, J. (1992) Mip protein of Legionella pneumophila exhibits peptidyl-prolyl-cis/trans isomerase (PPlase) activity. Mol Microbiol 6: 1375-1383.
    • (1992) Mol Microbiol , vol.6 , pp. 1375-1383
    • Fischer, G.1    Bang, H.2    Ludwig, B.3    Mann, K.4    Hacker, J.5
  • 10
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.-J., and Sambrook, J. (1992) Protein folding in the cell. Nature 355: 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.-J.1    Sambrook, J.2
  • 11
    • 0018365893 scopus 로고
    • A lipopolysaccharide binding cell surface protein from Salmonella minnesota. Isolation, partial characterization and occurence in different Enterobacteriaceae
    • Geyer, R., Galanos, C., Westphal, O., and Golecki, J.R. (1979) A lipopolysaccharide binding cell surface protein from Salmonella minnesota. Isolation, partial characterization and occurence in different Enterobacteriaceae. Eur J Biochem 98: 27-38.
    • (1979) Eur J Biochem , vol.98 , pp. 27-38
    • Geyer, R.1    Galanos, C.2    Westphal, O.3    Golecki, J.R.4
  • 12
    • 0025832204 scopus 로고
    • Lactococcal proteinase maturation protein PrtM is a lipoprotein
    • Haandrikman, A.J., Kok, J., and Venema, G. (1991) Lactococcal proteinase maturation protein PrtM is a lipoprotein. J Bacteriol 173: 4517-4525.
    • (1991) J Bacteriol , vol.173 , pp. 4517-4525
    • Haandrikman, A.J.1    Kok, J.2    Venema, G.3
  • 13
    • 0026059695 scopus 로고
    • The ompH gene of Yersinia enterocolitica: Cloning, sequencing, expression, and comparison with known enterobacterial ompH sequences
    • Hirvas, L., Koski, P., and Vaara, M. (1991) The ompH gene of Yersinia enterocolitica: cloning, sequencing, expression, and comparison with known enterobacterial ompH sequences. J Bacteriol 173: 1223-1239.
    • (1991) J Bacteriol , vol.173 , pp. 1223-1239
    • Hirvas, L.1    Koski, P.2    Vaara, M.3
  • 14
    • 0023814217 scopus 로고
    • Cloning and sequencing of the gene for the DNA binding 17K protein from Escherichia coli
    • Holck, A., and Kleppe, K. (1988) Cloning and sequencing of the gene for the DNA binding 17K protein from Escherichia coli. Gene 67: 117-124.
    • (1988) Gene , vol.67 , pp. 117-124
    • Holck, A.1    Kleppe, K.2
  • 15
    • 0029064061 scopus 로고
    • Escherichia coli and other species of Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins
    • Home, S.M., and Young, K.D. (1995) Escherichia coli and other species of Enterobacteriaceae encode a protein similar to the family of Mip-like FK506-binding proteins. Arch Microbiol 163: 357-365.
    • (1995) Arch Microbiol , vol.163 , pp. 357-365
    • Home, S.M.1    Young, K.D.2
  • 16
    • 0027264910 scopus 로고
    • Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized with or without prosequences
    • Jacobs, M., Andersen, J.B., Kontinen, V., and Sarvas, M. (1993) Bacillus subtilis PrsA is required in vivo as an extracytoplasmic chaperone for secretion of active enzymes synthesized with or without prosequences. Mol Microbiol 8: 957-966.
    • (1993) Mol Microbiol , vol.8 , pp. 957-966
    • Jacobs, M.1    Andersen, J.B.2    Kontinen, V.3    Sarvas, M.4
  • 17
    • 0023669069 scopus 로고
    • The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
    • Kohara, Y., Akiyama, K., and Isono, K. (1987) The physical map of the whole E. coli chromosome: application of a new strategy for rapid analysis and sorting of a large genomic library. Cell 50: 495-508.
    • (1987) Cell , vol.50 , pp. 495-508
    • Kohara, Y.1    Akiyama, K.2    Isono, K.3
  • 18
    • 0028297759 scopus 로고
    • Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12
    • Laird, M.W., Kloser, A.W., and Misra, R. (1994) Assembly of LamB and OmpF in deep rough lipopolysaccharide mutants of Escherichia coli K-12. J Bacteriol 176: 2259-2264.
    • (1994) J Bacteriol , vol.176 , pp. 2259-2264
    • Laird, M.W.1    Kloser, A.W.2    Misra, R.3
  • 19
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar, S., and Kolter, R. (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178: 1770-1773.
    • (1996) J Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.1    Kolter, R.2
  • 20
    • 0025059032 scopus 로고
    • Increased resolution of lipopolysaccharides and lipooligosaccharides utilizing tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis
    • Lesse, A.J., Campagnari, A.A., Bittner, W.E., and Apicella, M.A. (1990) Increased resolution of lipopolysaccharides and lipooligosaccharides utilizing tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis. J Immunol Meth 126: 109-117.
    • (1990) J Immunol Meth , vol.126 , pp. 109-117
    • Lesse, A.J.1    Campagnari, A.A.2    Bittner, W.E.3    Apicella, M.A.4
  • 21
    • 0025325366 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase from Escherichia coli: A periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A
    • Liu, J., and Walsh, C.T. (1990) Peptidyl-prolyl cis-trans isomerase from Escherichia coli: a periplasmic homolog of cyclophilin that is not inhibited by cyclosporin A. Proc Natl Acad Sci USA 87: 4028-4032.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4028-4032
    • Liu, J.1    Walsh, C.T.2
  • 22
    • 0027373949 scopus 로고
    • Crystal structure of the DsbA protein required for disulphide bond formation
    • Martin, J.L., Bardwell, J.C.A., and Kuriyan, J. (1993) Crystal structure of the DsbA protein required for disulphide bond formation. Nature 365: 464-467.
    • (1993) Nature , vol.365 , pp. 464-467
    • Martin, J.L.1    Bardwell, J.C.A.2    Kuriyan, J.3
  • 25
    • 0025768542 scopus 로고
    • A genetic approach for analysing the pathway of LamB assembly into the outer membrane of Escherichia coli
    • Misra, R., Peterson, A., Ferenci, T., and Silhavy, T.J. (1991) A genetic approach for analysing the pathway of LamB assembly into the outer membrane of Escherichia coli. J Biol Chem 266: 13592-13597.
    • (1991) J Biol Chem , vol.266 , pp. 13592-13597
    • Misra, R.1    Peterson, A.2    Ferenci, T.3    Silhavy, T.J.4
  • 26
    • 9444227193 scopus 로고    scopus 로고
    • Protein folding in E. coli periplasm
    • in press
    • Missiakas, D., and Raina, S. (1996) Protein folding in E. coli periplasm. J Bacteriol, in press.
    • (1996) J Bacteriol
    • Missiakas, D.1    Raina, S.2
  • 27
    • 0027291239 scopus 로고
    • Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulphide bonds in vivo
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1993) Identification and characterization of the Escherichia coli gene dsbB, whose product is involved in the formation of disulphide bonds in vivo. Proc Natl Acad Sci USA 90: 7084-7088.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7084-7088
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 28
    • 0028296940 scopus 로고
    • The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulphide bond formation
    • Missiakas, D., Georgopoulos, C., and Raina, S. (1994) The Escherichia coli dsbC (xprA) gene encodes a periplasmic protein involved in disulphide bond formation. EMBO J 13: 2013-2020.
    • (1994) EMBO J , vol.13 , pp. 2013-2020
    • Missiakas, D.1    Georgopoulos, C.2    Raina, S.3
  • 29
    • 0028979629 scopus 로고
    • Identification and characterization of a new disulphide isomerase-like protein (DsbD) in Escherichia coli
    • Missiakas, D., Schwager, F., and Raina, S. (1995) Identification and characterization of a new disulphide isomerase-like protein (DsbD) in Escherichia coli. EMBO J 14: 3415-3424.
    • (1995) EMBO J , vol.14 , pp. 3415-3424
    • Missiakas, D.1    Schwager, F.2    Raina, S.3
  • 31
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of sphaeroplasts
    • Neu, H.C., and Heppel, L.A. (1965) The release of enzymes from Escherichia coli by osmotic shock and during the formation of sphaeroplasts. J Biol Chem 240: 3685-3692.
    • (1965) J Biol Chem , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 32
    • 0021989093 scopus 로고
    • Molecular basis of bacterial outer membrane permeability
    • Nikaido, H., and Vaara, M. (1985) Molecular basis of bacterial outer membrane permeability. Microbiol Rev 49: 1-32.
    • (1985) Microbiol Rev , vol.49 , pp. 1-32
    • Nikaido, H.1    Vaara, M.2
  • 33
    • 0025284408 scopus 로고
    • Cloning, expression and characterization of the Escherichia coli K-12 rfaD gene
    • Pegues, J.C., Chen, L., Gordon, A.W., Ding, L., and Coleman, Jr, W.G. (1990) Cloning, expression and characterization of the Escherichia coli K-12 rfaD gene. J Bacteriol 172: 4652-4660.
    • (1990) J Bacteriol , vol.172 , pp. 4652-4660
    • Pegues, J.C.1    Chen, L.2    Gordon, A.W.3    Ding, L.4    Coleman Jr., W.G.5
  • 34
    • 0028124244 scopus 로고
    • Confirmation of the existence of a third family among peptidyl-prolyl cis/ trans isomerases: Amino acid sequence and recombinant production of parvulin
    • Rahfeld, J.-U., Rücknagel, K.P., Schelbert, B., Ludwig, B., Hacker, J., Mann, K., and Fischer, G. (1994a) Confirmation of the existence of a third family among peptidyl-prolyl cis/ trans isomerases: amino acid sequence and recombinant production of parvulin. FEBS Lett 352: 180-184.
    • (1994) FEBS Lett , vol.352 , pp. 180-184
    • Rahfeld, J.-U.1    Rücknagel, K.P.2    Schelbert, B.3    Ludwig, B.4    Hacker, J.5    Mann, K.6    Fischer, G.7
  • 35
    • 0028349613 scopus 로고
    • A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli
    • Rahfeld, J.-U., Schierhorn, A., Mann, K., and Fischer, G. (1994b) A novel peptidyl-prolyl cis/trans isomerase from Escherichia coli. FEBS Lett 343: 65-69.
    • (1994) FEBS Lett , vol.343 , pp. 65-69
    • Rahfeld, J.-U.1    Schierhorn, A.2    Mann, K.3    Fischer, G.4
  • 36
    • 0025744740 scopus 로고
    • The htrM gene, whose product is essential for Escherichia coli viability only at elevated temperatures, is identical to the rfaD gene
    • Raina, S., and Georgopoulos, C. (1991) The htrM gene, whose product is essential for Escherichia coli viability only at elevated temperatures, is identical to the rfaD gene. Nucl Acids Res 19: 3811-3819.
    • (1991) Nucl Acids Res , vol.19 , pp. 3811-3819
    • Raina, S.1    Georgopoulos, C.2
  • 37
    • 0025951604 scopus 로고
    • The Escherichia coli htrP gene product is essential for bacterial growth at high temperatures: Mapping, cloning, sequencing and transcriptional regulation of htrP
    • Raina, S., Mabey, L., and Georgopoulos, C. (1991) The Escherichia coli htrP gene product is essential for bacterial growth at high temperatures: mapping, cloning, sequencing and transcriptional regulation of htrP. J Bacteriol 173: 5999-6008.
    • (1991) J Bacteriol , vol.173 , pp. 5999-6008
    • Raina, S.1    Mabey, L.2    Georgopoulos, C.3
  • 39
    • 0025148584 scopus 로고
    • Role of lipopolysaccharide in assembly of Escherichia coli outer membrane proteins OmpA, OmpC, and OmpF
    • Ried, G., Hindennach, I., and Henning, U. (1990) Role of lipopolysaccharide in assembly of Escherichia coli outer membrane proteins OmpA, OmpC, and OmpF. J Bacteriol 172: 6048-6053.
    • (1990) J Bacteriol , vol.172 , pp. 6048-6053
    • Ried, G.1    Hindennach, I.2    Henning, U.3
  • 40
    • 0024730183 scopus 로고
    • Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12
    • Roa, B.B., Connolly, D.M., and Winkler, M.E. (1989) Overlap between pdxA and ksgA in the complex pdxA-ksgA-apaG-apaH operon of Escherichia coli K-12. J Bacteriol 171: 4767-4777.
    • (1989) J Bacteriol , vol.171 , pp. 4767-4777
    • Roa, B.B.1    Connolly, D.M.2    Winkler, M.E.3
  • 42
    • 0028348662 scopus 로고
    • Mutations in firA, encoding the second acyltransferase in lipopolysaccharide biosynthesis, affect multiple steps in lipopolysaccharide biosynthesis
    • Roy, A.M., and Coleman, J. (1994) Mutations in firA, encoding the second acyltransferase in lipopolysaccharide biosynthesis, affect multiple steps in lipopolysaccharide biosynthesis. J Bacteriol 176: 1639-1646.
    • (1994) J Bacteriol , vol.176 , pp. 1639-1646
    • Roy, A.M.1    Coleman, J.2
  • 45
    • 0027202811 scopus 로고
    • Genetics of lipopolysaccharide biosynthesis in enteric bacteria
    • Schnaitman, C.A., and Klena, J.D. (1993) Genetics of lipopolysaccharide biosynthesis in enteric bacteria. Microbiol Rev 57: 55-682.
    • (1993) Microbiol Rev , vol.57 , pp. 55-682
    • Schnaitman, C.A.1    Klena, J.D.2
  • 46
    • 0025970549 scopus 로고
    • Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin
    • Sen, K., and Nikaido, H. (1991) Lipopolysaccharide structure required for in vitro trimerization of Escherichia coli OmpF porin. J Bacteriol 173: 926-928.
    • (1991) J Bacteriol , vol.173 , pp. 926-928
    • Sen, K.1    Nikaido, H.2
  • 47
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller, G., Rücknagel, K.P., Nierhaus, K.H., Schmid, F.X., Fischer, G., and Rahfeld, J.-U. (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J 14: 4939-4948.
    • (1995) EMBO J , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rücknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.-U.6
  • 48
    • 0027530947 scopus 로고
    • Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy
    • Swain, L.A., Jaskolski, M., Housset, D., Rao, J.K.M., and Woldawer, A. (1993) Crystal structure of Escherichia coli L-asparaginase, an enzyme used in cancer therapy. Proc Natl Acad Sci USA 90: 1474-1478.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 1474-1478
    • Swain, L.A.1    Jaskolski, M.2    Housset, D.3    Rao, J.K.M.4    Woldawer, A.5
  • 49
    • 0026041449 scopus 로고
    • Skp is a periplasmic Escherichia coli protein requiring secA and SecY for export
    • Thome, B.M., and Muller, M. (1991) Skp is a periplasmic Escherichia coli protein requiring secA and SecY for export. Mol Microbiol 5: 2815-2817.
    • (1991) Mol Microbiol , vol.5 , pp. 2815-2817
    • Thome, B.M.1    Muller, M.2
  • 50
    • 0025309069 scopus 로고
    • surA, an Escherichia coli gene essential for survival in stationary phase
    • Tormo, A., Almiron, M., and Kolter, R. (1990) surA, an Escherichia coli gene essential for survival in stationary phase. J Bacteriol 172: 4339-4347.
    • (1990) J Bacteriol , vol.172 , pp. 4339-4347
    • Tormo, A.1    Almiron, M.2    Kolter, R.3
  • 51
    • 0025809486 scopus 로고
    • New pUC-derived cloning vectors with different selectable markers and DNA replication origins
    • Vieira, J., and Messing, J. (1991) New pUC-derived cloning vectors with different selectable markers and DNA replication origins. Gene 100: 189-194.
    • (1991) Gene , vol.100 , pp. 189-194
    • Vieira, J.1    Messing, J.2
  • 52
    • 0021681568 scopus 로고
    • New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition
    • Way, J.C., Davis, M.A., Morisato, D., Roberts, D.E., and Kleckner, N. (1984) New Tn10 derivatives for transposon mutagenesis and for construction of lacZ operon fusions by transposition. Gene 32: 369-379.
    • (1984) Gene , vol.32 , pp. 369-379
    • Way, J.C.1    Davis, M.A.2    Morisato, D.3    Roberts, D.E.4    Kleckner, N.5
  • 53
    • 84886622040 scopus 로고
    • An efficient and reproducible procedure for the formation of sphaeroplasts from variously grown Escherichia coli
    • Witholt, B.M., Boekhout, M., Brock, J., Kingma, H., Heerikhuizien, H., and Leu, L. (1976) An efficient and reproducible procedure for the formation of sphaeroplasts from variously grown Escherichia coli. Anal Biochem 74: 160-169.
    • (1976) Anal Biochem , vol.74 , pp. 160-169
    • Witholt, B.M.1    Boekhout, M.2    Brock, J.3    Kingma, H.4    Heerikhuizien, H.5    Leu, L.6
  • 55
    • 0028949156 scopus 로고
    • Structural and functional characterization of DsbC, a protein involved in disulphide bond formation in Escherichia coli
    • Zapun, A., Missiakas, D., Raina, S., and Creighton, T.E. (1995) Structural and functional characterization of DsbC, a protein involved in disulphide bond formation in Escherichia coli. Biochemistry 34: 5075-5089.
    • (1995) Biochemistry , vol.34 , pp. 5075-5089
    • Zapun, A.1    Missiakas, D.2    Raina, S.3    Creighton, T.E.4


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